The domain within your query sequence starts at position 396 and ends at position 438; the E-value for the EGF_CA domain shown below is 2.54e-7.

EGF_CA

A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown [(PUBMED:2288911), (PUBMED:6334307), (PUBMED:3534958), (PUBMED:6607417), (PUBMED:3282918)] to be present in a large number of membrane-bound and extracellular, mostly animal, proteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N terminus of some EGF-like domains [(PUBMED:1527084)]. Calcium-binding may be crucial for numerous protein-protein interactions.

For human coagulation factor IX it has been shown [(PUBMED:7606779)] that the calcium-ligands form a pentagonal bipyramid. The first, third and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) [(PUBMED:1527084)]. A conserved aromatic residue, as well as the second conserved negative residue, are thought to be involved in stabilising the calcium-binding site.

As in non-calcium binding EGF-like domains, there are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes [(PUBMED:1527084)].

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with EGF_CA domain which could be assigned to a KEGG orthologous group, and not all proteins containing EGF_CA domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.